scPDB - 2wat entry

Protein Data Bank Entry:

PDB ID : 2wat

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 2009-02-15

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Fatty acid synthase subunit alpha
ID:	FAS2_YEAST
AC:	P19097
Organism:	Saccharomyces cerevisiae
Reign:	Eukaryota
TaxID:	559292
EC Number:	2.3.1.86

Chains:

Chain Name:	Percentage of Residues within binding site
A	43 %
C	57 %

Ligand binding site composition:

B-Factor:	28.271
Number of residues:	54
Including
Standard Amino Acids:	50
Non Standard Amino Acids:	1
Water Molecules:	3
Cofactors:
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
0.738	853.875

% Hydrophobic	% Polar
32.81	67.19
According to VolSite

Ligand :

HET Code:	COA
Formula:	C21H32N7O16P3S
Molecular weight:	763.502 g/mol
DrugBank ID:	DB01992
Buried Surface Area:	59.72 %
Polar Surface area:	426.11 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	6
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	18

Mass center Coordinates

X	Y	Z
-29.1279	10.4252	-43.738

Binding mode :

What is Poseview ?

2D View
3D View

Image generated by PoseView

Protein

Binding Site

Ligand

Interaction pattern

hydrophobic (CA)

aromatic (CZ)

hydrogen bond acceptor (O)

hydrogen bond acceptor/donor (OG)

hydrogen bond donor (N)

positively ionized (NZ)

negatively ionized (OD1)

metal (ZN)

Legend:

Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand

Image generated using PoseView by BioSolveIT

Ligand	Protein		Interaction
Atom	Atom	Residue	Distance (Å)	Angle (°)	Type
CDP	CE2	PHE- 1820	4.04	0	Hydrophobic	false
CEP	CD2	PHE- 1820	3.73	0	Hydrophobic	false
O2A	NZ	LYS- 1821	3.04	145	H-Bond (Protein Donor)	false
O2A	NZ	LYS- 1821	3.04	0	Ionic (Protein Cationic)	false
CEP	CG	LYS- 1821	4.23	0	Hydrophobic	false
N6A	O	VAL- 1825	2.84	176.26	H-Bond (Ligand Donor)	false
CDP	CB	SER- 1827	4.32	0	Hydrophobic	false
O9P	OG	SER- 1827	2.6	148.25	H-Bond (Protein Donor)	false
O5P	N	LEU- 1828	2.9	166.39	H-Bond (Protein Donor)	false
C6P	CB	ALA- 1832	3.8	0	Hydrophobic	false
N4P	O	ALA- 1833	3.47	127.99	H-Bond (Ligand Donor)	false
C6P	CD2	LEU- 1834	3.73	0	Hydrophobic	false
C2P	CD2	LEU- 1834	4.34	0	Hydrophobic	false
O7A	NE	ARG- 1841	2.65	157.04	H-Bond (Protein Donor)	false
O7A	NH2	ARG- 1841	2.91	136.6	H-Bond (Protein Donor)	false
O8A	NH2	ARG- 1841	3.45	141.89	H-Bond (Protein Donor)	false
O7A	CZ	ARG- 1841	3.2	0	Ionic (Protein Cationic)	false
N6A	O	LYS- 1844	2.7	125.73	H-Bond (Ligand Donor)	false
C2B	CG	PRO- 1847	4.2	0	Hydrophobic	false
S1P	CB	ALA- 1855	3.98	0	Hydrophobic	false
O2A	OG	SER- 1872	2.78	177.33	H-Bond (Protein Donor)	false
O1A	N	HIS- 1873	2.86	152.26	H-Bond (Protein Donor)	false
O8A	O	HOH- 2034	2.55	146.82	H-Bond (Protein Donor)	false
N1A	O	HOH- 2086	2.68	179.97	H-Bond (Protein Donor)	false